HEADER CYTOKINE 22-AUG-25 9SGH TITLE BIMEKIZUMAB FAB IN COMPLEX WITH HUMAN INTERLEUKIN-17A COMPND MOL_ID: 1; COMPND 2 MOLECULE: BIMEKIZUMAB FAB HEAVY-CHAIN; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BIMEKIZUMAB FAB LIGHT-CHAIN; COMPND 7 CHAIN: B, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: INTERLEUKIN-17A; COMPND 11 CHAIN: I, J; COMPND 12 SYNONYM: IL-17,IL-17A,CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8, COMPND 13 CTLA-8; COMPND 14 ENGINEERED: YES; COMPND 15 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: IL17A, CTLA8, IL17; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 EXPRESSION_SYSTEM_VARIANT: STAR KEYWDS THERAPEUTIC ANTIBODY, CYTOKINE EXPDTA X-RAY DIFFRACTION AUTHOR J.-M.RONDEAU,S.LEHMANN REVDAT 1 29-OCT-25 9SGH 0 JRNL AUTH D.UNGAN,C.BE,P.BACZYK,S.MITTERMEIER,S.LEHMANN,C.WIESMANN, JRNL AUTH 2 T.HUBER,F.KOLBINGER,J.M.RONDEAU JRNL TITL IL-17A COMPLEXES WITH THERAPEUTIC ANTIBODIES EXHIBIT JRNL TITL 2 DISTINCT SIZE DISTRIBUTIONS, POTENTIALLY CONTRIBUTING TO JRNL TITL 3 CLINICALLY OBSERVED IMMUNOGENICITY. JRNL REF MABS V. 17 75840 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 41111004 JRNL DOI 10.1080/19420862.2025.2575840 REMARK 2 REMARK 2 RESOLUTION. 2.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.8 (26-JUL-2023) REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.09 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 71.8 REMARK 3 NUMBER OF REFLECTIONS : 33960 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1665 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.84 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 8.22 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 643 REMARK 3 BIN R VALUE (WORKING SET) : 0.3007 REMARK 3 BIN FREE R VALUE : 0.4102 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.44 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8341 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 11 REMARK 3 SOLVENT ATOMS : 71 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.09 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.64560 REMARK 3 B22 (A**2) : -1.93780 REMARK 3 B33 (A**2) : 2.58340 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.390 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 2.520 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.365 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 4.060 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.374 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 8581 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 11694 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2843 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1433 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8581 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1117 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 6082 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.93 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.15 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.85 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): -28.9127 -31.3988 -1.3935 REMARK 3 T TENSOR REMARK 3 T11: 0.1587 T22: -0.0211 REMARK 3 T33: -0.0751 T12: 0.0113 REMARK 3 T13: -0.0522 T23: 0.0265 REMARK 3 L TENSOR REMARK 3 L11: 0.7305 L22: 3.7624 REMARK 3 L33: 0.9642 L12: -1.1941 REMARK 3 L13: 0.2633 L23: 0.1568 REMARK 3 S TENSOR REMARK 3 S11: -0.0576 S12: 0.0422 S13: 0.2648 REMARK 3 S21: 0.3323 S22: 0.1007 S23: -0.1889 REMARK 3 S31: 0.3539 S32: 0.1600 S33: -0.0431 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): -34.7014 -41.8333 -16.1240 REMARK 3 T TENSOR REMARK 3 T11: 0.3222 T22: -0.1355 REMARK 3 T33: -0.1221 T12: 0.0893 REMARK 3 T13: -0.1106 T23: 0.0119 REMARK 3 L TENSOR REMARK 3 L11: 1.7666 L22: 5.6960 REMARK 3 L33: 0.1941 L12: -2.4940 REMARK 3 L13: 0.0796 L23: -0.6903 REMARK 3 S TENSOR REMARK 3 S11: 0.0846 S12: -0.0395 S13: 0.0673 REMARK 3 S21: -0.4165 S22: -0.0125 S23: 0.2913 REMARK 3 S31: 0.5984 S32: -0.0933 S33: -0.0721 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { H|* } REMARK 3 ORIGIN FOR THE GROUP (A): -29.0985 31.7109 -45.3222 REMARK 3 T TENSOR REMARK 3 T11: 0.0857 T22: -0.0245 REMARK 3 T33: -0.1359 T12: -0.0160 REMARK 3 T13: -0.0108 T23: 0.0305 REMARK 3 L TENSOR REMARK 3 L11: 1.4496 L22: 4.4386 REMARK 3 L33: 1.1587 L12: 1.3255 REMARK 3 L13: -0.1805 L23: 0.0091 REMARK 3 S TENSOR REMARK 3 S11: -0.0328 S12: -0.1069 S13: -0.1345 REMARK 3 S21: -0.3397 S22: -0.0357 S23: 0.0098 REMARK 3 S31: -0.2232 S32: 0.2443 S33: 0.0685 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { I|* } REMARK 3 ORIGIN FOR THE GROUP (A): -28.2419 -2.1915 -18.5237 REMARK 3 T TENSOR REMARK 3 T11: -0.3150 T22: -0.0128 REMARK 3 T33: 0.3699 T12: -0.0448 REMARK 3 T13: -0.0545 T23: 0.0770 REMARK 3 L TENSOR REMARK 3 L11: 7.2863 L22: 2.0530 REMARK 3 L33: 1.9275 L12: 0.8607 REMARK 3 L13: -1.5510 L23: -0.7038 REMARK 3 S TENSOR REMARK 3 S11: 0.3252 S12: -0.3492 S13: 0.2230 REMARK 3 S21: 0.1248 S22: -0.1455 S23: -0.4245 REMARK 3 S31: -0.0610 S32: 0.3854 S33: -0.1797 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { J|* } REMARK 3 ORIGIN FOR THE GROUP (A): -28.7784 1.7292 -29.7381 REMARK 3 T TENSOR REMARK 3 T11: -0.2858 T22: 0.0084 REMARK 3 T33: 0.3538 T12: 0.0220 REMARK 3 T13: 0.0379 T23: 0.1424 REMARK 3 L TENSOR REMARK 3 L11: 8.2552 L22: 1.8002 REMARK 3 L33: 1.9306 L12: -1.5007 REMARK 3 L13: 0.9227 L23: -0.1540 REMARK 3 S TENSOR REMARK 3 S11: 0.1663 S12: 0.2562 S13: 0.2457 REMARK 3 S21: -0.2426 S22: -0.0651 S23: -0.4191 REMARK 3 S31: 0.0331 S32: 0.3969 S33: -0.1012 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { L|* } REMARK 3 ORIGIN FOR THE GROUP (A): -35.3804 41.9855 -30.5239 REMARK 3 T TENSOR REMARK 3 T11: 0.2752 T22: -0.1314 REMARK 3 T33: -0.0890 T12: -0.0777 REMARK 3 T13: 0.0644 T23: -0.0000 REMARK 3 L TENSOR REMARK 3 L11: 1.6664 L22: 6.0457 REMARK 3 L33: 0.4144 L12: 2.3707 REMARK 3 L13: -0.1463 L23: -0.2769 REMARK 3 S TENSOR REMARK 3 S11: 0.0675 S12: -0.0722 S13: 0.0425 REMARK 3 S21: 0.3332 S22: 0.0352 S23: 0.4841 REMARK 3 S31: -0.5932 S32: -0.0837 S33: -0.1026 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS CARRIED OUT AGAINST REMARK 3 STARANISO DATA. ELLIPSOIDAL COMPLETENESS WAS 93.9% OVERALL. REMARK 4 REMARK 4 9SGH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1292150377. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-SEP-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.99989 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC 1.1.7 (20230726) REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.1.7 (20230726) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33970 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.661 REMARK 200 RESOLUTION RANGE LOW (A) : 92.755 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 200 DATA REDUNDANCY : 10.60 REMARK 200 R MERGE (I) : 0.27700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92 REMARK 200 COMPLETENESS FOR SHELL (%) : 58.8 REMARK 200 DATA REDUNDANCY IN SHELL : 13.10 REMARK 200 R MERGE FOR SHELL (I) : 2.29100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.92 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M ZINC ACETATE, 0.1M IMIDAZOLE PH REMARK 280 6.5, 10% PEG 8,000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 58.78100 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.24600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.78100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.24600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I, J, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH I 306 LIES ON A SPECIAL POSITION. REMARK 375 HOH J 306 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 141 REMARK 465 SER A 142 REMARK 465 THR A 143 REMARK 465 SER A 144 REMARK 465 GLY A 145 REMARK 465 SER A 227 REMARK 465 CYS A 228 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 THR A 231 REMARK 465 HIS A 232 REMARK 465 SER H 140 REMARK 465 LYS H 141 REMARK 465 SER H 142 REMARK 465 THR H 143 REMARK 465 SER H 144 REMARK 465 GLY H 145 REMARK 465 GLY H 146 REMARK 465 SER H 227 REMARK 465 CYS H 228 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 PRO I 34 REMARK 465 ASN I 35 REMARK 465 SER I 36 REMARK 465 GLU I 37 REMARK 465 ASP I 38 REMARK 465 ASN I 53 REMARK 465 ARG I 54 REMARK 465 ASN I 55 REMARK 465 THR I 56 REMARK 465 ASN I 57 REMARK 465 THR I 58 REMARK 465 ASN I 59 REMARK 465 PRO I 60 REMARK 465 LYS I 61 REMARK 465 ARG I 62 REMARK 465 SER I 63 REMARK 465 SER I 64 REMARK 465 VAL I 154 REMARK 465 ALA I 155 REMARK 465 PRO J 34 REMARK 465 ASN J 35 REMARK 465 SER J 36 REMARK 465 GLU J 37 REMARK 465 ASP J 38 REMARK 465 LYS J 39 REMARK 465 ASN J 40 REMARK 465 ASN J 53 REMARK 465 ARG J 54 REMARK 465 ASN J 55 REMARK 465 THR J 56 REMARK 465 ASN J 57 REMARK 465 THR J 58 REMARK 465 ASN J 59 REMARK 465 PRO J 60 REMARK 465 LYS J 61 REMARK 465 ARG J 62 REMARK 465 SER J 63 REMARK 465 VAL J 154 REMARK 465 ALA J 155 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ARG A 109 35.81 -78.19 REMARK 500 ASP A 156 70.01 52.79 REMARK 500 ARG B 30 -104.70 53.77 REMARK 500 VAL B 51 -55.84 73.47 REMARK 500 SER B 67 128.07 -176.85 REMARK 500 ARG H 109 35.60 -79.45 REMARK 500 ASP H 156 70.97 63.25 REMARK 500 SER I 72 71.41 -118.09 REMARK 500 SER J 72 71.29 -117.22 REMARK 500 GLU J 83 38.78 -95.31 REMARK 500 ARG L 30 -110.60 51.90 REMARK 500 VAL L 51 -54.80 72.77 REMARK 500 SER L 77 88.88 -150.30 REMARK 500 ASN L 152 -4.52 77.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 54 OE1 REMARK 620 2 HOH A 308 O 41.6 REMARK 620 3 ASP B 151 OD2 43.0 2.4 REMARK 620 4 HIS B 189 ND1 43.3 1.8 2.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU H 54 OE1 REMARK 620 2 GLU H 54 OE2 56.6 REMARK 620 3 HOH H 405 O 95.6 75.0 REMARK 620 4 ASP L 151 OD2 40.4 29.5 62.7 REMARK 620 5 HIS L 189 ND1 38.7 32.0 62.8 2.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN I 202 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS I 96 NE2 REMARK 620 2 HOH I 310 O 87.8 REMARK 620 3 HOH I 313 O 107.2 143.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN I 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP I 103 OD2 REMARK 620 2 ASP I 107 OD2 21.1 REMARK 620 3 HIS I 109 ND1 25.1 10.8 REMARK 620 4 HOH I 312 O 37.8 18.5 13.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN J 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS J 96 NE2 REMARK 620 2 HOH J 308 O 80.5 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN J 202 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP J 103 OD2 REMARK 620 2 ASP J 107 OD2 31.1 REMARK 620 3 HIS J 109 ND1 37.1 11.6 REMARK 620 N 1 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9SFX RELATED DB: PDB REMARK 900 SECUKINUMAB FV COMPLEX WITH HUMAN IL-17A REMARK 900 RELATED ID: 9SG0 RELATED DB: PDB REMARK 900 CJM112 FV COMPLEX WITH HUMAN IL-17A REMARK 900 RELATED ID: 9SG2 RELATED DB: PDB REMARK 900 IXEKIZUMAB FAB COMPLEX WITH HUMAN IL-17A DBREF 9SGH A 1 232 PDB 9SGH 9SGH 1 232 DBREF 9SGH B 1 213 PDB 9SGH 9SGH 1 213 DBREF 9SGH H 1 232 PDB 9SGH 9SGH 1 232 DBREF 9SGH I 34 155 UNP Q16552 IL17_HUMAN 34 155 DBREF 9SGH J 34 155 UNP Q16552 IL17_HUMAN 34 155 DBREF 9SGH L 1 213 PDB 9SGH 9SGH 1 213 SEQADV 9SGH SER I 129 UNP Q16552 CYS 129 ENGINEERED MUTATION SEQADV 9SGH SER J 129 UNP Q16552 CYS 129 ENGINEERED MUTATION SEQRES 1 A 232 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 232 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 232 PHE THR PHE SER ASP TYR ASN MET ALA TRP VAL ARG GLN SEQRES 4 A 232 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA THR ILE THR SEQRES 5 A 232 TYR GLU GLY ARG ASN THR TYR TYR ARG ASP SER VAL LYS SEQRES 6 A 232 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 A 232 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 232 ALA VAL TYR TYR CYS ALA SER PRO PRO GLN TYR TYR GLU SEQRES 9 A 232 GLY SER ILE TYR ARG LEU TRP PHE ALA HIS TRP GLY GLN SEQRES 10 A 232 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 232 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 232 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 232 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 232 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 232 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 232 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 232 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 232 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 B 213 ALA ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA ASP SEQRES 3 B 213 GLU SER VAL ARG THR LEU MET HIS TRP TYR GLN GLN LYS SEQRES 4 B 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LEU VAL SER SEQRES 5 B 213 ASN SER GLU ILE GLY VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 B 213 GLY SER GLY THR ASP PHE ARG LEU THR ILE SER SER LEU SEQRES 7 B 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN THR SEQRES 8 B 213 TRP SER ASP PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 B 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 213 PHE ASN ARG GLY GLU SEQRES 1 H 232 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 232 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 232 PHE THR PHE SER ASP TYR ASN MET ALA TRP VAL ARG GLN SEQRES 4 H 232 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA THR ILE THR SEQRES 5 H 232 TYR GLU GLY ARG ASN THR TYR TYR ARG ASP SER VAL LYS SEQRES 6 H 232 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 232 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 232 ALA VAL TYR TYR CYS ALA SER PRO PRO GLN TYR TYR GLU SEQRES 9 H 232 GLY SER ILE TYR ARG LEU TRP PHE ALA HIS TRP GLY GLN SEQRES 10 H 232 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 232 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 232 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 232 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 232 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 232 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 232 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 232 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 232 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 I 122 PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET SEQRES 2 I 122 VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN SEQRES 3 I 122 PRO LYS ARG SER SER ASP TYR TYR ASN ARG SER THR SER SEQRES 4 I 122 PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR SEQRES 5 I 122 PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY SEQRES 6 I 122 CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SEQRES 7 I 122 SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG SEQRES 8 I 122 GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS SEQRES 9 I 122 ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE SEQRES 10 I 122 VAL HIS HIS VAL ALA SEQRES 1 J 122 PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET SEQRES 2 J 122 VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN SEQRES 3 J 122 PRO LYS ARG SER SER ASP TYR TYR ASN ARG SER THR SER SEQRES 4 J 122 PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR SEQRES 5 J 122 PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY SEQRES 6 J 122 CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SEQRES 7 J 122 SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG SEQRES 8 J 122 GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS SEQRES 9 J 122 ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE SEQRES 10 J 122 VAL HIS HIS VAL ALA SEQRES 1 L 213 ALA ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA ASP SEQRES 3 L 213 GLU SER VAL ARG THR LEU MET HIS TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LEU VAL SER SEQRES 5 L 213 ASN SER GLU ILE GLY VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR ASP PHE ARG LEU THR ILE SER SER LEU SEQRES 7 L 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN THR SEQRES 8 L 213 TRP SER ASP PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 213 PHE ASN ARG GLY GLU HET ZN B 301 1 HET ZN H 301 1 HET ZN I 201 1 HET ZN I 202 1 HET PO4 I 203 5 HET ZN J 201 1 HET ZN J 202 1 HETNAM ZN ZINC ION HETNAM PO4 PHOSPHATE ION FORMUL 7 ZN 6(ZN 2+) FORMUL 11 PO4 O4 P 3- FORMUL 14 HOH *71(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASP A 62 LYS A 65 5 4 HELIX 3 AA3 ASN A 74 LYS A 76 5 3 HELIX 4 AA4 ARG A 87 THR A 91 5 5 HELIX 5 AA5 SER A 168 ALA A 170 5 3 HELIX 6 AA6 SER A 199 LEU A 201 5 3 HELIX 7 AA7 LYS A 213 ASN A 216 5 4 HELIX 8 AA8 GLN B 79 PHE B 83 5 5 HELIX 9 AA9 SER B 121 LYS B 126 1 6 HELIX 10 AB1 LYS B 183 HIS B 189 1 7 HELIX 11 AB2 THR H 28 TYR H 32 5 5 HELIX 12 AB3 ASP H 62 LYS H 65 5 4 HELIX 13 AB4 ASN H 74 LYS H 76 5 3 HELIX 14 AB5 ARG H 87 THR H 91 5 5 HELIX 15 AB6 SER H 168 ALA H 170 5 3 HELIX 16 AB7 PRO H 197 LEU H 201 5 5 HELIX 17 AB8 LYS H 213 ASN H 216 5 4 HELIX 18 AB9 TYR I 66 SER I 70 1 5 HELIX 19 AC1 ASP J 65 SER J 70 1 6 HELIX 20 AC2 GLN L 79 PHE L 83 5 5 HELIX 21 AC3 SER L 121 LYS L 126 1 6 HELIX 22 AC4 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 SER A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AA2 6 ALA A 92 SER A 98 -1 N TYR A 94 O THR A 119 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O TYR A 59 N THR A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AA3 4 ALA A 92 SER A 98 -1 N TYR A 94 O THR A 119 SHEET 4 AA3 4 HIS A 114 TRP A 115 -1 O HIS A 114 N SER A 98 SHEET 1 AA4 4 SER A 132 LEU A 136 0 SHEET 2 AA4 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AA4 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AA4 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AA5 4 SER A 132 LEU A 136 0 SHEET 2 AA5 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AA5 4 TYR A 188 PRO A 197 -1 O LEU A 190 N VAL A 154 SHEET 4 AA5 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AA6 3 THR A 163 TRP A 166 0 SHEET 2 AA6 3 TYR A 206 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AA6 3 THR A 217 VAL A 223 -1 O VAL A 223 N TYR A 206 SHEET 1 AA7 4 LEU B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 SER B 10 SER B 14 0 SHEET 2 AA8 6 THR B 102 LYS B 107 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 6 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA8 6 MET B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ASN B 53 SER B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AA9 4 SER B 10 SER B 14 0 SHEET 2 AA9 4 THR B 102 LYS B 107 1 O GLU B 105 N LEU B 11 SHEET 3 AA9 4 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA9 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AB1 4 TYR B 173 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AB1 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB2 4 ALA B 153 LEU B 154 0 SHEET 2 AB2 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB2 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 4 AB2 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB3 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB3 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB4 6 LEU H 11 VAL H 12 0 SHEET 2 AB4 6 THR H 119 VAL H 123 1 O THR H 122 N VAL H 12 SHEET 3 AB4 6 ALA H 92 SER H 98 -1 N TYR H 94 O THR H 119 SHEET 4 AB4 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB4 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB4 6 THR H 58 TYR H 60 -1 O TYR H 59 N THR H 50 SHEET 1 AB5 4 LEU H 11 VAL H 12 0 SHEET 2 AB5 4 THR H 119 VAL H 123 1 O THR H 122 N VAL H 12 SHEET 3 AB5 4 ALA H 92 SER H 98 -1 N TYR H 94 O THR H 119 SHEET 4 AB5 4 HIS H 114 TRP H 115 -1 O HIS H 114 N SER H 98 SHEET 1 AB6 4 SER H 132 LEU H 136 0 SHEET 2 AB6 4 ALA H 148 TYR H 157 -1 O LEU H 153 N PHE H 134 SHEET 3 AB6 4 TYR H 188 VAL H 196 -1 O LEU H 190 N VAL H 154 SHEET 4 AB6 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AB7 4 SER H 132 LEU H 136 0 SHEET 2 AB7 4 ALA H 148 TYR H 157 -1 O LEU H 153 N PHE H 134 SHEET 3 AB7 4 TYR H 188 VAL H 196 -1 O LEU H 190 N VAL H 154 SHEET 4 AB7 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AB8 3 THR H 163 TRP H 166 0 SHEET 2 AB8 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AB8 3 THR H 217 VAL H 223 -1 O VAL H 219 N VAL H 210 SHEET 1 AB9 8 ARG I 84 TYR I 85 0 SHEET 2 AB9 8 ASN I 111 ARG I 124 -1 O LEU I 122 N TYR I 85 SHEET 3 AB9 8 SER I 132 VAL I 147 -1 O GLY I 143 N ILE I 115 SHEET 4 AB9 8 THR J 44 ASN J 48 1 O MET J 46 N PHE I 133 SHEET 5 AB9 8 THR I 44 ASN I 48 -1 N VAL I 47 O VAL J 45 SHEET 6 AB9 8 SER J 132 VAL J 147 1 O LEU J 135 N ASN I 48 SHEET 7 AB9 8 ASN J 111 ARG J 124 -1 N ASN J 111 O VAL J 147 SHEET 8 AB9 8 ARG J 84 TYR J 85 -1 N TYR J 85 O LEU J 122 SHEET 1 AC1 2 TRP I 74 GLU I 80 0 SHEET 2 AC1 2 VAL I 88 CYS I 94 -1 O GLU I 91 N HIS I 77 SHEET 1 AC2 2 CYS I 99 ILE I 100 0 SHEET 2 AC2 2 VAL I 106 ASP I 107 -1 O ASP I 107 N CYS I 99 SHEET 1 AC3 2 TRP J 74 GLU J 80 0 SHEET 2 AC3 2 VAL J 88 CYS J 94 -1 O GLU J 91 N HIS J 77 SHEET 1 AC4 2 CYS J 99 ILE J 100 0 SHEET 2 AC4 2 VAL J 106 ASP J 107 -1 O ASP J 107 N CYS J 99 SHEET 1 AC5 4 LEU L 4 SER L 7 0 SHEET 2 AC5 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AC5 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AC5 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AC6 6 SER L 10 SER L 14 0 SHEET 2 AC6 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC6 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AC6 6 MET L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AC6 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC6 6 ASN L 53 SER L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AC7 4 SER L 10 SER L 14 0 SHEET 2 AC7 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC7 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AC7 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AC8 4 SER L 114 PHE L 118 0 SHEET 2 AC8 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AC8 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AC8 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AC9 4 ALA L 153 LEU L 154 0 SHEET 2 AC9 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AC9 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AC9 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.06 SSBOND 2 CYS A 152 CYS A 208 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.06 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.05 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 6 CYS H 152 CYS H 208 1555 1555 2.03 SSBOND 7 CYS I 94 CYS I 144 1555 1555 2.03 SSBOND 8 CYS I 99 CYS I 146 1555 1555 2.04 SSBOND 9 CYS J 94 CYS J 144 1555 1555 2.03 SSBOND 10 CYS J 99 CYS J 146 1555 1555 2.04 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 12 CYS L 134 CYS L 194 1555 1555 2.05 LINK OE1 GLU A 54 ZN ZN B 301 1555 3455 2.08 LINK O HOH A 308 ZN ZN B 301 3445 1555 2.19 LINK OD2 ASP B 151 ZN ZN B 301 1555 1555 1.89 LINK ND1 HIS B 189 ZN ZN B 301 1555 1555 2.12 LINK OE1 GLU H 54 ZN ZN H 301 1555 1555 2.29 LINK OE2 GLU H 54 ZN ZN H 301 1555 1555 2.37 LINK ZN ZN H 301 O HOH H 405 1555 1555 2.43 LINK ZN ZN H 301 OD2 ASP L 151 3454 1555 2.23 LINK ZN ZN H 301 ND1 HIS L 189 3454 1555 2.22 LINK NE2 HIS I 96 ZN ZN I 202 1555 1555 2.19 LINK OD2 ASP I 103 ZN ZN I 201 1555 2455 2.42 LINK OD2 ASP I 107 ZN ZN I 201 1555 1555 1.86 LINK ND1 HIS I 109 ZN ZN I 201 1555 1555 1.95 LINK ZN ZN I 201 O HOH I 312 1555 1555 2.61 LINK ZN ZN I 202 O HOH I 310 1555 1555 2.47 LINK ZN ZN I 202 O HOH I 313 1555 1555 2.60 LINK NE2 HIS J 96 ZN ZN J 201 1555 1555 2.25 LINK OD2 ASP J 103 ZN ZN J 202 1555 2455 2.27 LINK OD2 ASP J 107 ZN ZN J 202 1555 1555 1.87 LINK ND1 HIS J 109 ZN ZN J 202 1555 1555 1.98 LINK ZN ZN J 201 O HOH J 308 1555 1555 2.45 CISPEP 1 PHE A 158 PRO A 159 0 -2.66 CISPEP 2 GLU A 160 PRO A 161 0 6.61 CISPEP 3 SER B 7 PRO B 8 0 -1.41 CISPEP 4 ASP B 94 PRO B 95 0 -3.91 CISPEP 5 TYR B 140 PRO B 141 0 1.64 CISPEP 6 PHE H 158 PRO H 159 0 -3.40 CISPEP 7 GLU H 160 PRO H 161 0 3.26 CISPEP 8 TYR I 85 PRO I 86 0 -3.63 CISPEP 9 GLU I 125 PRO I 126 0 0.51 CISPEP 10 TYR J 85 PRO J 86 0 -0.47 CISPEP 11 GLU J 125 PRO J 126 0 0.56 CISPEP 12 SER L 7 PRO L 8 0 -1.73 CISPEP 13 ASP L 94 PRO L 95 0 -3.37 CISPEP 14 TYR L 140 PRO L 141 0 1.79 CRYST1 117.562 148.492 92.755 90.00 90.00 90.00 P 21 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008506 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006734 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010781 0.00000